Detection of a gonococcal endo-beta-N-acetyl-D-glucosaminidase and its peptidoglycan cleavage site.
Neisseria gonorrhoeae contains several hydrolases which may be responsible for gonococcal cell lysis. One of these enzymes, an endo-beta-N-acetyl-D-glucosaminidase, has been extracted from supernatants of sonicated gonococci and partially purified by ammonium sulfate precipitation and affinity and ion-exchange chromatography. This enzyme has a different specificity than egg white lysozyme and cleaves the beta 1 leads to 4 glycosidic linkage between N-acetylglucosamine and N-acetylmuramic acid in gonococcal peptidoglycan.
D000118:Acetylglucosaminidase / Q000302:isolation & purification / Q000378:metabolism*; D006596:Hexosaminidases / Q000378:metabolism*; D007700:Kinetics; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D009344:Neisseria gonorrhoeae / Q000201:enzymology*; D010457:Peptidoglycan; D013379:Substrate Specificity
D010457:Peptidoglycan; D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase